6U6P

Solution NMR Structure Of The Full Length Latent Form MinE Protein From Neisseria gonorrheae

6U6P の概要

• エントリーDOI: 10.2210/pdb6u6p/pdb
• NMR情報: BMRB: 30661
• 分子名称: Cell division topological specificity factor (1 entity in total)
• 機能のキーワード: mind, mine, cell division, cell cycle
• 由来する生物種: Neisseria gonorrhoeae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18513.45

構造登録者

Cai, M.,Shen, Y.,Clore, M. (登録日: 2019-08-30, 公開日: 2020-07-08, 最終更新日: 2024-05-01)

主引用文献

Cai, M.,Huang, Y.,Shen, Y.,Li, M.,Mizuuchi, M.,Ghirlando, R.,Mizuuchi, K.,Clore, G.M.
Probing transient excited states of the bacterial cell division regulator MinE by relaxation dispersion NMR spectroscopy.
Proc.Natl.Acad.Sci.USA, 116:25446-25455, 2019

PubMed Abstract: Bacterial MinD and MinE form a standing oscillatory wave which positions the cell division inhibitor MinC, that binds MinD, everywhere on the membrane except at the midpoint of the cell, ensuring midcell positioning of the cytokinetic septum. During this process MinE undergoes fold switching as it interacts with different partners. We explore the exchange dynamics between major and excited states of the MinE dimer in 3 forms using N relaxation dispersion NMR: the full-length protein (6-stranded β-sheet sandwiched between 4 helices) representing the resting state; a 10-residue N-terminal deletion (Δ10) mimicking the membrane-binding competent state where the N-terminal helix is detached to interact with membrane; and N-terminal deletions of either 30 (Δ30) or 10 residues with an I24N mutation (Δ10/I24N), in which the β1-strands at the dimer interface are extruded and available to bind MinD, leaving behind a 4-stranded β-sheet. Full-length MinE samples 2 "excited" states: The first is similar to a full-length/Δ10 heterodimer; the second, also sampled by Δ10, is either similar to or well along the pathway toward the 4-stranded β-sheet form. Both Δ30 and Δ10/I24N sample 2 excited species: The first may involve destabilization of the β3- and β3'-strands at the dimer interface; changes in the second are more extensive, involving further disruption of secondary structure, possibly representing an ensemble of states on the pathway toward restoration of the resting state. The quantitative information on MinE conformational dynamics involving these excited states is crucial for understanding the oscillation pattern self-organization by MinD-MinE interaction dynamics on the membrane.

PubMed: 31772021
DOI: 10.1073/pnas.1915948116

実験手法

SOLUTION NMR